IN 1928 the Worshipful Company of Clothworkers of the City of London made a grant of £3,000 a year to the University of Leeds for research purposes. Never has a grant been more fully justified, for it resulted in the appointment of Dr. W. T. Astbury as lecturer in textile physics and induced him to take up the study of proteins. A scholar of Jesus College, Cambridge, Astbury had acted as assistant to Sir William Bragg, first at University College, London, during 1921–23, and then at the Davy Faraday Laboratory of the Royal Institution during 1923–28. At Leeds, therefore, X-ray studies of hair, wool and related fibres claimed his immediate attention, and the main features of the molecular structure of the keratins were defined in two papers published in the Philosophical Transactions of the Royal Society in 1931 and 1933. The industrial importance of this and other work was recognized by the award of the Gold Medal of the Worshipful Company of Dyers in 1934, and the Warner Memorial Medal of the Textile Institute in 1935. Its implications in the biological field were even more profound: assisted by generous grants from the Rockefeller Foundation since 1933, he utilized his concept of folded and, extended poly-peptide chains, derived from the examination of unstretched and stretched wool fibres, to obtain a structural interpretation of the denaturation phenomenon, and, later, to identify the keratins, myosin, fibrinogen and fibrin as belonging to the same group of proteins.